9NQY
Nipah Virus Matrix Lattice in Complex with Human Cell Membrane
Summary for 9NQY
| Entry DOI | 10.2210/pdb9nqy/pdb |
| EMDB information | 49696 |
| Descriptor | Matrix protein (1 entity in total) |
| Functional Keywords | assembly lattice, virus like particle |
| Biological source | Henipavirus nipahense |
| Total number of polymer chains | 18 |
| Total formula weight | 802061.64 |
| Authors | |
| Primary citation | Upadhye, V.V.,Lee, J.F.,Ercanli, N.,Ricana, C.,Hinsley, A.C.,Obr, M.,Autin, L.,Schur, F.K.M.,Aguilar, H.C.,Dick, R.A. Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles. Biorxiv, 2026 Cited by PubMed Abstract: Nipah virus (NiV) is a BSL-4 zoonotic paramyxovirus with ~75% human mortality. The matrix protein (M) of NiV and other paramyxoviruses binds the inner leaflet of the cellular plasma membrane, orchestrating virion assembly by bringing together transmembrane glycoproteins (F/G) and ribonucleoprotein complexes (N). However, the interactions of these full-length proteins within membrane complexes remain elusive. Using cryo-electron tomography and subtomogram averaging of virus like particles (VLPs), we interrogated the protein:protein interactions of the main NiV structural proteins M/N/F/G. The M lattice structure determined to 7Å revealed a novel M-dimer arrangement that yielded two distinct repeating holes. Notably, F-trimers were arranged above only one of the two holes, dependent on F's cytoplasmic tail. G was enriched in regions of higher M-VLP curvature, while N dramatically increased M-VLP pleomorphism. This work provides novel insights into paramyxoviral protein complexes, structures, and morphology. PubMed: 42523209DOI: 10.64898/2026.07.16.738223 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7 Å) |
Structure validation
Download full validation report
